5kcy

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<StructureSection load='5kcy' size='340' side='right'caption='[[5kcy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5kcy' size='340' side='right'caption='[[5kcy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspte Aspte]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KCY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kcy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus Aspergillus terreus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KCY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GST:GERANYL+S-THIOLODIPHOSPHATE'>GST</scene>, <scene name='pdbligand=XBU:METHYL+(2~{R})-3-(4-HYDROXYPHENYL)-2-[(4-HYDROXYPHENYL)METHYL]-4-OXIDANYL-5-OXIDANYLIDENE-FURAN-2-CARBOXYLATE'>XBU</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kcg|5kcg]], [[5kcl|5kcl]], [[5kcq|5kcq]], [[5kd0|5kd0]], [[5kd6|5kd6]], [[5kda|5kda]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GST:GERANYL+S-THIOLODIPHOSPHATE'>GST</scene>, <scene name='pdbligand=XBU:METHYL+(2~{R})-3-(4-HYDROXYPHENYL)-2-[(4-HYDROXYPHENYL)METHYL]-4-OXIDANYL-5-OXIDANYLIDENE-FURAN-2-CARBOXYLATE'>XBU</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kcy OCA], [http://pdbe.org/5kcy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kcy RCSB], [http://www.ebi.ac.uk/pdbsum/5kcy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kcy ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kcy OCA], [https://pdbe.org/5kcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kcy RCSB], [https://www.ebi.ac.uk/pdbsum/5kcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kcy ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1B0UHJ4_ASPTE A0A1B0UHJ4_ASPTE]
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Aromatic prenyltransferases (aPTases) transfer prenyl moieties from isoprenoid donors to various aromatic acceptors, some of which have the rare property of extreme enzymatic promiscuity toward both a variety of prenyl donors and a large diversity of acceptors. In this study, we discovered a new aPTase, AtaPT, from Aspergillus terreus that exhibits unprecedented promiscuity toward diverse aromatic acceptors and prenyl donors and also yields products with a range of prenylation patterns. Systematic crystallographic studies revealed various discrete conformations for ligand binding with donor-dependent acceptor specificity and multiple binding sites within a spacious hydrophobic substrate-binding pocket. Further structure-guided mutagenesis of active sites at the substrate-binding pocket is responsible for altering the specificity and promiscuity toward substrates and the diversity of product prenylations. Our study reveals the molecular mechanism underlying the promiscuity of AtaPT and suggests an efficient protein engineering strategy to generate new prenylated derivatives in drug discovery applications.
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Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase.,Chen R, Gao B, Liu X, Ruan F, Zhang Y, Lou J, Feng K, Wunsch C, Li SM, Dai J, Sun F Nat Chem Biol. 2017 Feb;13(2):226-234. doi: 10.1038/nchembio.2263. Epub 2016 Dec , 19. PMID:27992881<ref>PMID:27992881</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kcy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspte]]
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[[Category: Aspergillus terreus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, B]]
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[[Category: Gao B]]
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[[Category: Sun, F]]
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[[Category: Sun F]]
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[[Category: Abba fold]]
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[[Category: Substrate promiscuity]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the aromatic prenyltransferase AtaPT from Aspergillus terreus A8-4 in complex with geranyl S-thiolodiphosphate and (+)-butyrolactone II

PDB ID 5kcy

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OCA

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